Key result
The individual N- or C-lobes of calmodulin bind to Cav1.2 in a Ca(2+)-dependent manner and rescue the basal activity of the channel from run-down in guinea-pig ventricular myocytes.
Individual N- and C-lobes of calmodulin can independently tether to Cav1.2 channels and rescue their basal activity from run-down in guinea-pig ventricular myocytes.
Lobe-specific calmodulin effects on Cav1.2 in rodent myocytes extend mechanistic models; leaves open human translation and therapeutic relevance.
The present study examined the binding of the individual N- and C-lobes of calmodulin (CaM) to Cav1.2 at different Ca(2+) concentration ([Ca(2+)]) from ≈ free to 2mM, and found that they may bind to Cav1.2 Ca(2+)-dependently. In particular, using the patch-clamp technique, we confirmed that the N- or C-lobes can rescue the basal activity of Cav1.2 from run-down, demonstrating the functional relevance of the individual lobes. The data imply that at resting [Ca(2+)], CaM may tether to the channel with its single lobe, leading to multiple CaM molecule binding to increase the grade of Ca(2+)-dependent regulation of Cav1.2.
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Shao et al. (2014) studied this question. N- and C-lobes of calmodulin (CaM) was evaluated on Binding to Cav1.2 and rescue of basal activity from run-down. The individual N- or C-lobes of calmodulin bind to Cav1.2 in a Ca(2+)-dependent manner and rescue the basal activity of the channel from run-down in guinea-pig ventricular myocytes.
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